title: Isolation, purification, crystallization and preliminary crystallographic studies of a chitinase from Crocus vernus.
abstract: A chitinase has been isolated and purified from Crocus vernus corms. N-terminal amino-acid sequence analysis of the approximately 30 kDa protein showed 33% identity to narbonin, a seed protein from Vicia narbonensis L. The C. vernus chitinase was crystallized by the hanging-drop vapour-diffusion method using PEG 8000 as the main precipitant. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=172.3, b=37.1, c=126.4 Å, β=127° and two molecules per asymmetric unit. Diffraction data were collected to a resolution of 2.1 Å.
authors.affiliation: Department of Chemistry, University of Hamburg, c/o DESY, Laboratory for Structural Biology of Infection and Inflammation, Notkestrasse 85, 22603 Hamburg, Germany.
authors.forename: Ahmed
authors.initials: A
authors.lastname: Akrem
authors.forename: Sadaf
authors.initials: S
authors.lastname: Iqbal
authors.forename: Friedrich
authors.initials: F
authors.lastname: Buck
authors.forename: Arne
authors.initials: A
authors.lastname: Meyer
authors.forename: Markus
authors.initials: M
authors.lastname: Perbandt
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Voelter
authors.forename: Christian
authors.initials: C
authors.lastname: Betzel
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002688:Chitinases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D027622:Crocus / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D005916:Globulins / Q000235:genetics; D008969:Molecular Sequence Data; D014674:Plant Proteins, Dietary / Q000235:genetics; D016415:Sequence Alignment; D014961:X-Ray Diffraction
chemical_list: D005916:Globulins; D014674:Plant Proteins, Dietary; C066193:narbonin; D002688:Chitinases